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4 Answers to end-of-chapter questions

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Structured questions
9

Succinic acid

[1]

Malonic acid is a competitive inhibitor


Since it has a similar structure to succinic acid the substrate it competes for the
active site and binds to it
Less substrate (succinic acid) attaches to the active site of enzyme
Less product (fumaric acid) is formed
Explanation [2]
malonic acid
competitive
inhibitor, similar
shape to substrate

substrate
succinic acid

enzyme succinic
dehydrogenase

inhibitor binds to
active site hence no
enzymesubstrate
complex formed; no
products formed

Diagram only [1]


Explanation on diagram [3]
Max [3]
c

Ethanol has a similar molecular structure to ethylene glycol /


substrate
Therefore, it would also be complementary to the active site of
enzyme
Ethanol would act as a competitive inhibitor
It would compete for the active site of enzyme
It would prevent ethylene glycol (the substrate) from binding with
active site

Biology for CAPE

56 points [3]

Original material Cambridge University Press 2011

Fewer enzymesubstrate complexes and less product (oxalic acid)


formed

Heavy metals form covalent bonds with the SH groups of the


enzyme
These bonds may be formed in the active site
If bonds are formed at the active site, the active site would be
permanently blocked
So no enzymesubstrate complexes could be formed
If the covalent bonds with the heavy metal and SH groups
are formed away from the active site (at allosteric site),
these bonds would disrupt the tertiary structure of the
enzyme
This would change the shape of the active site
Hence the active site would no longer be complementary to
substrate
Substrate would no longer be able to fit in the active site
(lock and key)
Or the active site would be prevented from changing shape
to fit the substrate (induced fit)
Well explained with
No enzymesubstrate complexes formed hence no
either bond formation at
products
the active site or elsewhere [2]

34 points [2]
12 points [1]

heavy metal permanently bonded at


the active site so substrate no
longer fits in the active site

substrate no longer fits in


the active site

shape of the active site


changes

Good diagram [2]


e

Biology for CAPE

Original material Cambridge University Press 2011

Rate of reaction

(b)

(d)

Substrate concentration
10 a
b

Each curve [2]

Metabolic reactions the chemical reactions occurring within an organisms body

[2]

Lock-and-key
The substrate molecule is complementary in shape to that of the
active site
The active site on the surface of the enzyme is so contoured and
charged that it attracts only one substrate and the shape of the
active site is complementary to that of the substrate
It was thought that the substrate exactly fitted into the active site
of the enzyme molecule like a key fitting into a lock (lock-andkey theory)
Enzymesubstrate complexes formed
This explained why an enzyme would only work on one
substrate (specificity)

[2]

Induced fit
Active site is not perfectly contoured to fit substrate
When the substrate attaches to the active site, the shape of the
whole enzyme changes slightly so it can accommodate and hold
the substrate

[1]

From 10 C to 41 C , the rate of activity increases from 0% to 100%


For every 10 C increase in temperature, the activity doubled
Rate increased because there is more kinetic energy
Enzyme and substrate molecules collide more often, also
because more molecules have sufficient energy to overcome the
activation energy
Optimum is 41 C
Above the optimum temperature, the rate decreases as more of
the enzyme molecules denature
The thermal energy breaks the hydrogen bonds holding the
secondary and tertiary structure of the enzyme together
So the enzyme loses its shape and becomes a random coil and
the substrate can no longer fit into the active site
This is irreversible
5 points well explained [5]

Biology for CAPE

Original material Cambridge University Press 2011

ii

COO
NH2

COOH
+
NH3

inactive

11 a

active

inactive

Diagram [3]
Correct activity [2]

disappearance of substrate
appearance of product

Biology for CAPE

[1]
[1]

Original material Cambridge University Press 2011

at 22 C

x-axis labelled, with appropriate intervals [1]


y-axis, with appropriate intervals [1]
Points correctly plotted and joined [1]
Title [1]

Graph showing the effect of pH on enzyme activity


of catalase
ii

iii

optimum pH = 7
lowest activity is at pH 3
active over a narrow range
increasing activity as pH increases to optimum / pH 7
decreasing activity as pH increases above optimum / pH 7

45 points [2]
23 points [1]

At pH 3
high concentration of H+ ions
enzyme acts a buffer
COOH groups unionized
H and ionic bonds broken
tertiary structure of enzyme disrupted
shape of active site changes
few enzymesubstrate complexes formed

[1]

At pH 7
optimum activity: active site unchanged, enzymesubstrate complexes formed,
maximum products

[1]

At pH 8
low concentration of H+ ions
enzyme acts a buffer
NH2 groups unionised
Hydrogen bonds and ionic interactions broken
tertiary structure of enzyme disrupted
shape of active site changes
few enzymesubstrate complexes formed

[1]

Biology for CAPE

Original material Cambridge University Press 2011

See graph above: same basic shape / lower activity

[2]

To maintain the pH of each experimental solution

[1]

volume of hydrogen peroxide used


volume of enzyme used
time for reaction to take place

Any 2 points [1]

Essay questions
12 a

Activation energy is the minimum free energy that must be


possessed by the molecules on collision for the particles to react
It is the amount of energy needed to raise the reactants to an
activated state
It is amount of energy given temporarily to a substrate to be
converted into a product

Any point [2]

ii

Each curve [1]


b

Enzyme has tertiary structure


Active site of enzyme is made up of few amino acids
With a specific shape
Shape of active site complementary to substrate
Only one substrate or type of substrate will fit into active site
To form enzymesubstrate complexes
Refer to lock-and-key and induced fit

7 points [4]
56 points [3]
34 points [2]
12 points [1]

Substrate binds to active site of enzyme


Few amino acids are involved
Remainder of amino acids maintains the globular shape
Shape of active site complementary to substrate
Can interact by exact fit: lock-and-key
Then moulds around the substrate: induced fit
Substrate held to active site by hydrogen bonds and ionic
interactions bonds as well as hydrophobic and hydrophilic
interactions
To form the enzymesubstrate complex

Biology for CAPE

Original material Cambridge University Press 2011

13 a

Enzymesubstrate complex activated into forming products


Substrate changes shape slightly
To put strain on bonds in the substrate / weakens bonds
Activated into forming products
Which no longer fit the active site
Products move way, leaving the active site free to
form more enzymesubstrate complexes

pH

Each point [1]


Max [7]

Well drawn and labelled [1]


Description
Normally enzyme works in narrow pH range
Rate reduces quickly when pH changes from optimum pH

[1]

Explanation
Changes in pH from optimum affect H+ ion concentration in solution
At low PH
high concentration of H+ ions
enzyme acts a buffer
COOH groups unionised
At high pH
low concentration of H+ ions
enzyme acts a buffer
NH2 groups unionised
Hydrogen bonds and ionic interactions
In both cases
tertiary structure of enzyme disrupted
shape of active site changes
few enzymesubstrate complexes formed

[2]

ii

Enzyme concentration

Biology for CAPE

Original material Cambridge University Press 2011

Well drawn and labelled [1]


Description
Rate of reaction increases as enzyme concentration increases
Rate directly proportional / linear to enzyme concentration

[1]

Explanation
More active sites are available
More collisions between enzyme and substrate molecules
More enzymesubstrate complexes formed
More product as enzyme concentration increases

[2]

iii

Substrate concentration

Well drawn and labelled [1]


Description
Initial substrate concentration limits the rate of reaction / rate directly proportional
to substrates concentration
Reaches maximum velocity and plateaus
[1]
Explanation
All active sites initially available
More frequent collisions between substrate and active sites
Then as substrate concentration increases, all active sites become occupied /
saturated
No more enzymesubstrate complexes can be formed until product is formed.
iv

[2]

Inhibitors

Biology for CAPE

Original material Cambridge University Press 2011

Well drawn and labelled [1]


Description
Inhibitor reduces rate of reaction
Can be competitive or non-competitive
Can be reversible or irreversible

[1]

Explanation
Competitive
similar shape to substrate
competes for active site / occupies active site / binds at active site
blocks entry of substrate
less substrate bind / less enzymesubstrate complex formed
does not bind permanently to active site
increasing concentration lessens effect of inhibitor
Non-competitive
not similar in shape to substrate
binds permanently to active site and blocks it
hence irreversible
or binds to a site away from active site / allosteric site
this distorts the tertiary structure of the enzyme
shape of active site changes
this could be reversible or irreversible
increasing substrate concentration does not lessen
effect of inhibitor
b

Held in place in active site by temporary bonds


e.g. hydrogen, ionic, hydrophobic and hydrophilic interactions
That form between the substrate and some of the R groups of the
enzymes amino acids

Biology for CAPE

Well explained [2]

1 point each [max 3]

Original material Cambridge University Press 2011

14 a

optimum temperature = 40 C: more kinetic energy,


more collisions between enzyme and substrate,
more enzymesubstrate complexes formed

at low temperatures:
slow reaction; less
kinetic energy; fewer
collisions between
enzyme and substrate;
fewer enzyme
substrate complexes
formed, enzyme is not
denatured; for every
10 C increase in
temperature, rate

temperature above
optimum: more kinetic
energy; molecules
vibrate quickly;
hydrogen bonds broken
in tertiary structure of
enzyme; shape of
active site changes;
fewer/no enzyme
substrate complexes
formed; enzyme
denatured; irreversible
Graph [1]
Annotations [3]

General class is hydrolases


For proteins (e.g. blood and grass): proteases
Grease/oil: lipases
Starch-based products (e.g. gravy / sauces): amylases

ii

ii

Example [1]

Temperature between 40 C and 50 C


Conditions [2]
Cleaning power depends on enzyme activity
Optimum temperature for enzyme
Maximum collisions between enzyme and substrate
More products
Substrate / stain broken down
Neutral pH / detergent and water only
If pH decreases from optimum, H+ ions would interact with amino acids of
enzymes
Hydrogen bonds and ionic interactions broken
Tertiary structure of enzyme disrupted
Shape of active site changes
Few enzymesubstrate complexes formed
Well explained [3]
Non-competitive inhibition
Tertiary structure of enzyme distorted when aspirin attaches to R group of
amino acid of enzyme
Changes shape of active site
Substrate for COX no longer fits in active site
No enzymesubstrate complexes formed
Well explained [2]

Competitive inhibition occurring


Since penicillin resembles the substrate
It is also irreversible since bonds permanently at the active site
Therefore stops activity of transpeptidase

Biology for CAPE

General class [1]

Well explained [2]

Original material Cambridge University Press 2011

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